ID A0A0B3RIQ6_9RHOB Unreviewed; 335 AA.
AC A0A0B3RIQ6; A0A225PHW5;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Thiamine pyrimidine synthase {ECO:0000256|ARBA:ARBA00033171};
GN ORFNames=KU6B_48780 {ECO:0000313|EMBL:BBU58613.1}, OA50_04181
GN {ECO:0000313|EMBL:KHQ51150.1};
OS Mameliella alba.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Mameliella.
OX NCBI_TaxID=561184 {ECO:0000313|EMBL:KHQ51150.1, ECO:0000313|Proteomes:UP000030960};
RN [1] {ECO:0000313|EMBL:KHQ51150.1, ECO:0000313|Proteomes:UP000030960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMTAT08 {ECO:0000313|EMBL:KHQ51150.1,
RC ECO:0000313|Proteomes:UP000030960};
RA Gan H.Y., Muhd D.-D., Mohd Noor M.E., Yeong Y.S., Usup G.;
RT "Genome sequence of Ponticoccus sp. strain UMTAT08 isolated from clonal
RT culture of toxic dinoflagellate Alexandrium tamiyavanichii.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BBU58613.1, ECO:0000313|Proteomes:UP000501194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KU6B {ECO:0000313|EMBL:BBU58613.1,
RC ECO:0000313|Proteomes:UP000501194};
RA Iwaki H.;
RT "Complete genome sequence of Mameliella alba strain KU6B, a
RT cyclohexylamine-degrading marine bacterium.";
RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(3+) + 4 H2O + L-histidyl-[4-amino-5-hydroxymethyl-2-
CC methylpyrimidine phosphate synthase] + N(6)-(pyridoxal phosphate)-L-
CC lysyl-[4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase]
CC = (2S)-2-amino-5-hydroxy-4-oxopentanoyl-[4-amino-5-hydroxymethyl-2-
CC methylpyrimidine phosphate synthase] + 3-oxopropanoate + 4-amino-2-
CC methyl-5-(phosphooxymethyl)pyrimidine + 2 Fe(2+) + 2 H(+) + L-lysyl-
CC [4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase];
CC Xref=Rhea:RHEA:65756, Rhea:RHEA-COMP:16892, Rhea:RHEA-COMP:16893,
CC Rhea:RHEA-COMP:16894, Rhea:RHEA-COMP:16895, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:29979, ChEBI:CHEBI:33190,
CC ChEBI:CHEBI:58354, ChEBI:CHEBI:143915, ChEBI:CHEBI:157692;
CC Evidence={ECO:0000256|ARBA:ARBA00023967};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65757;
CC Evidence={ECO:0000256|ARBA:ARBA00023967};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004948}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the NMT1/THI5 family.
CC {ECO:0000256|ARBA:ARBA00009406}.
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DR EMBL; AP022337; BBU58613.1; -; Genomic_DNA.
DR EMBL; JSUQ01000019; KHQ51150.1; -; Genomic_DNA.
DR RefSeq; WP_043144903.1; NZ_QAOY01000026.1.
DR AlphaFoldDB; A0A0B3RIQ6; -.
DR STRING; 561184.SAMN05216376_12512; -.
DR GeneID; 66503969; -.
DR KEGG; malu:KU6B_48780; -.
DR PATRIC; fig|1515334.3.peg.4218; -.
DR OrthoDB; 9815602at2; -.
DR Proteomes; UP000030960; Unassembled WGS sequence.
DR Proteomes; UP000501194; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR027939; NMT1/THI5.
DR InterPro; IPR015168; SsuA/THI5.
DR PANTHER; PTHR31528; 4-AMINO-5-HYDROXYMETHYL-2-METHYLPYRIMIDINE PHOSPHATE SYNTHASE THI11-RELATED; 1.
DR PANTHER; PTHR31528:SF1; 4-AMINO-5-HYDROXYMETHYL-2-METHYLPYRIMIDINE PHOSPHATE SYNTHASE THI11-RELATED; 1.
DR Pfam; PF09084; NMT1; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000030960};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..335
FT /note="Thiamine pyrimidine synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033714682"
FT DOMAIN 38..252
FT /note="SsuA/THI5-like"
FT /evidence="ECO:0000259|Pfam:PF09084"
SQ SEQUENCE 335 AA; 35343 MW; 14F69370734AECEA CRC64;
MIKQTFAALA ATVALSGAAL AETAVPFALD WKFEGPAAPY FVAIDDGYFG EQDLSVEISA
GQGSLDAIPK VATGAFPVGF ADINSLIKFL DQNPGAPVTA VMMIYDKPPF AVVGRKSLGV
EAPKDLEGKV LGAPPPDGAW AQFPAFASAN DLDMSKITVE PVGFPTREPM LAEGNVAAIT
GFSFSSYLNL VRLGVPEDDI STILMADHGL QLYGNAIIVN TDYAAENPEI ITGFLTAIAA
GWKDAIADPA GAIESLMTRN PAADADLEQR RLQLSIDANV LTDYAETNGM GGIDPARLDV
ALEQLAETYE FQNAPDASLY FTDAYLPDAA ARMLK
//
